UniProtKB - P07101 (TY3H_HUMAN)
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- BLAST>sp|P07101|TY3H_HUMAN Tyrosine 3-monooxygenase OS=Homo sapiens OX=9606 GN=TH PE=1 SV=5 MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTP RSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPR ATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVR QVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEI AFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNI PQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCC HELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYG AGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYAS RIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
- Align
Tyrosine 3-monooxygenase
TH
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: dopamine biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes dopamine from L-tyrosine.Proteins known to be involved in the 2 steps of the subpathway in this organism are:
- Tyrosine 3-monooxygenase (TH)
- Aromatic-L-amino-acid decarboxylase (DDC)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dopamine from L-tyrosine, the pathway dopamine biosynthesis and in Catecholamine biosynthesis.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 361 | IronBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 366 | IronBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 406 | IronBy similarity | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- amino acid binding Source: Ensembl
- dopamine binding Source: Ensembl
- enzyme binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ferric iron binding Source: Ensembl
- ferrous iron binding Source: Ensembl
- oxygen binding Source: Ensembl
- protein domain specific binding Source: Ensembl
- tetrahydrobiopterin binding Source: Ensembl
- tyrosine 3-monooxygenase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- aminergic neurotransmitter loading into synaptic vesicle Source: Ensembl
- anatomical structure morphogenesis Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- animal organ morphogenesis Source: BHF-UCL
- catecholamine biosynthetic process Source: Reactome
- cellular response to alkaloid Source: Ensembl
- cellular response to glucose stimulus Source: Ensembl
- cellular response to growth factor stimulus Source: Ensembl
- cellular response to manganese ion Source: Ensembl
- cellular response to nicotine Source: Ensembl
- cerebral cortex development Source: Ensembl
- circadian sleep/wake cycle Source: Ensembl
- dopamine biosynthetic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- dopamine biosynthetic process from tyrosine Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- eating behavior Source: Ensembl
- embryonic camera-type eye morphogenesis Source: BHF-UCL
- epinephrine biosynthetic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- eye photoreceptor cell development Source: BHF-UCL
- fatty acid metabolic process Source: Ensembl
- glycoside metabolic process Source: Ensembl
- heart development Source: BHF-UCL
- heart morphogenesis Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- isoquinoline alkaloid metabolic process Source: Ensembl
- learning Source: BHF-UCL
- locomotory behavior Source: BHF-UCL
- mating behavior Source: Ensembl
- memory Source: BHF-UCL
- multicellular organism aging Source: Ensembl
- neurotransmitter biosynthetic process Source: UniProtKB-KW
- norepinephrine biosynthetic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- phthalate metabolic process Source: Ensembl
- phytoalexin metabolic process Source: Ensembl
- pigmentation Source: BHF-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of heart contraction Source: BHF-UCL
- response to activity Source: Ensembl
- response to amphetamine Source: Ensembl
- response to corticosterone Source: Ensembl
- response to electrical stimulus Source: Ensembl
- response to estradiol Source: Ensembl
- response to ethanol Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to ether Source: Ensembl
- response to herbicide Source: Ensembl
- response to hypoxia Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to immobilization stress Source: Ensembl
- response to isolation stress Source: Ensembl
- response to light stimulus Source: Ensembl
- response to lipopolysaccharide Source: Ensembl
- response to nutrient levels Source: Ensembl
- response to peptide hormone Source: Ensembl
- response to pyrethroid Source: Ensembl
- response to salt stress Source: Ensembl
- response to water deprivation Source: Ensembl
- response to zinc ion Source: Ensembl
- sensory perception of sound Source: Ensembl
- social behavior Source: Ensembl
- sphingolipid metabolic process Source: Ensembl
- synaptic transmission, dopaminergic Source: BHF-UCL
- terpene metabolic process Source: Ensembl
- visual perception Source: BHF-UCL
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Monooxygenase, Oxidoreductase |
| Biological process | Catecholamine biosynthesis, Neurotransmitter biosynthesis |
| Ligand | Iron, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.14.16.2 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-209905 Catecholamine biosynthesis |
SIGNOR Signaling Network Open Resource More...SIGNORi | P07101 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00747; UER00733 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Tyrosine 3-monooxygenase (EC:1.14.16.2)Alternative name(s): Tyrosine 3-hydroxylase Short name: TH |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:TH Synonyms:TYH |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000180176.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11782 TH |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 191290 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P07101 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cytosol
- cytosol Source: Reactome
Endoplasmic reticulum
- smooth endoplasmic reticulum Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Mitochondrion
- mitochondrion Source: Ensembl
Nucleus
- nucleus Source: BHF-UCL
Plasma Membrane
- cytoplasmic side of plasma membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cytoplasmic vesicle Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- dendrite Source: Ensembl
- melanosome membrane Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neuron projection Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- perikaryon Source: BHF-UCL
- synaptic vesicle Source: Ensembl
- terminal bouton Source: Ensembl
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Segawa syndrome autosomal recessive (ARSEGS)23 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.13"A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome."
Luedecke B., Dworniczak B., Bartholome K.
Hum. Genet. 95:123-125(1995) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN ARSEGS, VARIANT ARSEGS LYS-412. - Ref.15"Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene."
Knappskog P.M., Flatmark T., Mallet J., Luedecke B., Bartholome K.
Hum. Mol. Genet. 4:1209-1212(1995) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT ARSEGS LYS-412. - Ref.16"Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene."
Luedecke B., Knappskog P.M., Clayton P.T., Surtees R.A.H., Clelland J.D., Heales S.J.R., Brand M.P., Bartholome K., Flatmark T.
Hum. Mol. Genet. 5:1023-1028(1996) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT ARSEGS PRO-236. - Ref.17"Association study of structural mutations of the tyrosine hydroxylase gene with schizophrenia and Parkinson's disease."
Kunugi H., Kawada Y., Hattori M., Ueki A., Otsuka M., Nanko S.
Am. J. Med. Genet. 81:131-133(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ARSEGS PRO-236, VARIANT MET-112. - Ref.19"A common point mutation in the tyrosine hydroxylase gene in autosomal recessive L-DOPA-responsive dystonia in the Dutch population."
van den Heuvel L.P.W.J., Luiten B., Smeitink J.A.M., de Rijk-van Andel J.F., Hyland K., Steenbergen-Spanjers G.C.H., Janssen R.J.T., Wevers R.A.
Hum. Genet. 102:644-646(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ARSEGS HIS-233. - Ref.20"Biochemical and molecular genetic characteristics of the severe form of tyrosine hydroxylase deficiency."
Braeutigam C., Steenbergen-Spanjers G.C., Hoffmann G.F., Dionisi-Vici C., van den Heuvel L.P., Smeitink J.A., Wevers R.A.
Clin. Chem. 45:2073-2078(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ARSEGS PHE-359. - Ref.22"Four novel mutations in the tyrosine hydroxylase gene in patients with infantile parkinsonism."
Swaans R.J.M., Rondot P., Renier W.O., Van Den Heuvel L.P.W.J., Steenbergen-Spanjers G.C.H., Wevers R.A.
Ann. Hum. Genet. 64:25-31(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS PRO-276; MET-314; HIS-337 AND MET-494. - Ref.23"Tyrosine hydroxylase deficiency unresponsive to L-dopa treatment with unusual clinical and biochemical presentation."
De Lonlay P., Nassogne M.C., van Gennip A.H., van Cruchten A.C., Billatte de Villemeur T., Cretz M., Stoll C., Launay J.M., Steenberger-Spante G.C., van den Heuvel L.P., Wevers R.A., Saudubray J.M., Abeling N.G.
J. Inherit. Metab. Dis. 23:819-825(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ARSEGS SER-309. - Ref.24"Long-term course of L-dopa-responsive dystonia caused by tyrosine hydroxylase deficiency."
Schiller A., Wevers R.A., Steenbergen G.C., Blau N., Jung H.H.
Neurology 63:1524-1526(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS VAL-376 AND GLY-498. - Ref.25"Levodopa-responsive infantile parkinsonism due to a novel mutation in the tyrosine hydroxylase gene and exacerbation by viral infections."
Diepold K., Schuetz B., Rostasy K., Wilken B., Hougaard P., Guettler F., Romstad A., Birk Moeller L.
Mov. Disord. 20:764-767(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS TYR-246 AND GLY-498. - Ref.26"Pre- and postnatal diagnosis of tyrosine hydroxylase deficiency."
Moeller L.B., Romstad A., Paulsen M., Hougaard P., Ormazabal A., Pineda M., Blau N., Guettler F., Artuch R.
Prenat. Diagn. 25:671-675(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS TRP-328 AND MET-399. - Ref.27"Mutations in the cyclic adenosine monophosphate response element of the tyrosine hydroxylase gene."
Verbeek M.M., Steenbergen-Spanjers G.C., Willemsen M.A., Hol F.A., Smeitink J., Seeger J., Grattan-Smith P., Ryan M.M., Hoffmann G.F., Donati M.A., Blau N., Wevers R.A.
Ann. Neurol. 62:422-426(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS MET-387 AND LEU-492. - Ref.28"Tyrosine hydroxylase deficiency presenting with a biphasic clinical course."
Giovanniello T., Leuzzi V., Carducci C., Carducci C., Sabato M.L., Artiola C., Santagata S., Pozzessere S., Antonozzi I.
Neuropediatrics 38:213-215(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS ARG-414 AND GLN-510. - Ref.29"Molecular analyses of GCH-1, TH and parkin genes in Chinese dopa-responsive dystonia families."
Wu Z.Y., Lin Y., Chen W.J., Zhao G.X., Xie H., Murong S.X., Wang N.
Clin. Genet. 74:513-521(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS HIS-233 AND SER-247. - Ref.30"Exhaustive analysis of BH4 and dopamine biosynthesis genes in patients with Dopa-responsive dystonia."
Clot F., Grabli D., Cazeneuve C., Roze E., Castelnau P., Chabrol B., Landrieu P., Nguyen K., Ponsot G., Abada M., Doummar D., Damier P., Gil R., Thobois S., Ward A.J., Hutchinson M., Toutain A., Picard F. , Camuzat A., Fedirko E., San C., Bouteiller D., LeGuern E., Durr A., Vidailhet M., Brice A.
Brain 132:1753-1763(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS ALA-301; PRO-319; LEU-375; ARG-414 AND GLY-467. - Ref.31"Tyrosine hydroxylase deficiency: a treatable disorder of brain catecholamine biosynthesis."
Willemsen M.A., Verbeek M.M., Kamsteeg E.J., de Rijk-van Andel J.F., Aeby A., Blau N., Burlina A., Donati M.A., Geurtz B., Grattan-Smith P.J., Haeussler M., Hoffmann G.F., Jung H., de Klerk J.B., van der Knaap M.S., Kok F., Leuzzi V., de Lonlay P. , Megarbane A., Monaghan H., Renier W.O., Rondot P., Ryan M.M., Seeger J., Smeitink J.A., Steenbergen-Spanjers G.C., Wassmer E., Weschke B., Wijburg F.A., Wilcken B., Zafeiriou D.I., Wevers R.A.
Brain 133:1810-1822(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS TYR-207; GLY-227; THR-241; GLY-259 AND THR-394. - Ref.32"Biochemical and molecular characterization of tyrosine hydroxylase deficiency in Hong Kong Chinese."
Mak C.M., Lam C.W., Siu T.S., Chan K.Y., Siu W.K., Yeung W.L., Hui J., Wong V.C., Low L.C., Ko C.H., Fung C.W., Chen S.P., Yuen Y.P., Lee H.C., Yau E., Chan B., Tong S.F., Tam S., Chan Y.W.
Mol. Genet. Metab. 99:431-433(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS ARG-294; SER-315; VAL-385; THR-394 AND ARG-408. - Ref.33"A novel compound heterozygous tyrosine hydroxylase mutation (p.R441P) with complex phenotype."
Haugarvoll K., Bindoff L.A.
J. Parkinson's Dis. 1:119-122(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS PRO-441 AND GLY-498. - Ref.34"A new tyrosine hydroxylase genotype associated with early-onset severe encephalopathy."
Giovanniello T., Claps D., Carducci C., Carducci C., Blau N., Vigevano F., Antonozzi I., Leuzzi V.
J. Child Neurol. 27:523-525(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS LEU-251; PHE-279 AND GLN-296, VARIANT MET-112. - Ref.35"Myoclonus-dystonia syndrome due to tyrosine hydroxylase deficiency."
Stamelou M., Mencacci N.E., Cordivari C., Batla A., Wood N.W., Houlden H., Hardy J., Bhatia K.P.
Neurology 79:435-441(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ARSEGS ARG-428. - Ref.36"Tyrosine hydroxylase deficiency in Taiwanese infants."
Chi C.S., Lee H.F., Tsai C.R.
Pediatr. Neurol. 46:77-82(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARSEGS HIS-233; SER-315 AND THR-382. - Ref.37"GTP cyclohydrolase I and tyrosine hydroxylase gene mutations in familial and sporadic dopa-responsive dystonia patients."
Cai C., Shi W., Zeng Z., Zhang M., Ling C., Chen L., Cai C., Zhang B., Li W.D.
PLoS ONE 8:E65215-E65215(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CYS-19 AND ARG-428. - Ref.38"Functional studies of tyrosine hydroxylase missense variants reveal distinct patterns of molecular defects in Dopa-responsive dystonia."
Fossbakk A., Kleppe R., Knappskog P.M., Martinez A., Haavik J.
Hum. Mutat. 35:880-890(2014) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS ARSEGS TYR-207; GLY-227; HIS-233; PRO-236; THR-241; TYR-246; SER-247; GLY-259; PRO-276; ALA-301; SER-309; MET-314; PRO-319; TRP-328; HIS-337; PHE-359; LEU-375; VAL-376; MET-387; THR-394; MET-399; LYS-412; ARG-414; PRO-441; GLY-467; LEU-492; MET-494; GLY-498 AND GLN-510.
Luedecke B., Dworniczak B., Bartholome K.
Hum. Genet. 95:123-125(1995) [PubMed] [Europe PMC] [Abstract]
Knappskog P.M., Flatmark T., Mallet J., Luedecke B., Bartholome K.
Hum. Mol. Genet. 4:1209-1212(1995) [PubMed] [Europe PMC] [Abstract]
Luedecke B., Knappskog P.M., Clayton P.T., Surtees R.A.H., Clelland J.D., Heales S.J.R., Brand M.P., Bartholome K., Flatmark T.
Hum. Mol. Genet. 5:1023-1028(1996) [PubMed] [Europe PMC] [Abstract]
Kunugi H., Kawada Y., Hattori M., Ueki A., Otsuka M., Nanko S.
Am. J. Med. Genet. 81:131-133(1998) [PubMed] [Europe PMC] [Abstract]
van den Heuvel L.P.W.J., Luiten B., Smeitink J.A.M., de Rijk-van Andel J.F., Hyland K., Steenbergen-Spanjers G.C.H., Janssen R.J.T., Wevers R.A.
Hum. Genet. 102:644-646(1998) [PubMed] [Europe PMC] [Abstract]
Braeutigam C., Steenbergen-Spanjers G.C., Hoffmann G.F., Dionisi-Vici C., van den Heuvel L.P., Smeitink J.A., Wevers R.A.
Clin. Chem. 45:2073-2078(1999) [PubMed] [Europe PMC] [Abstract]
Swaans R.J.M., Rondot P., Renier W.O., Van Den Heuvel L.P.W.J., Steenbergen-Spanjers G.C.H., Wevers R.A.
Ann. Hum. Genet. 64:25-31(2000) [PubMed] [Europe PMC] [Abstract]
De Lonlay P., Nassogne M.C., van Gennip A.H., van Cruchten A.C., Billatte de Villemeur T., Cretz M., Stoll C., Launay J.M., Steenberger-Spante G.C., van den Heuvel L.P., Wevers R.A., Saudubray J.M., Abeling N.G.
J. Inherit. Metab. Dis. 23:819-825(2000) [PubMed] [Europe PMC] [Abstract]
Schiller A., Wevers R.A., Steenbergen G.C., Blau N., Jung H.H.
Neurology 63:1524-1526(2004) [PubMed] [Europe PMC] [Abstract]
Diepold K., Schuetz B., Rostasy K., Wilken B., Hougaard P., Guettler F., Romstad A., Birk Moeller L.
Mov. Disord. 20:764-767(2005) [PubMed] [Europe PMC] [Abstract]
Moeller L.B., Romstad A., Paulsen M., Hougaard P., Ormazabal A., Pineda M., Blau N., Guettler F., Artuch R.
Prenat. Diagn. 25:671-675(2005) [PubMed] [Europe PMC] [Abstract]
Verbeek M.M., Steenbergen-Spanjers G.C., Willemsen M.A., Hol F.A., Smeitink J., Seeger J., Grattan-Smith P., Ryan M.M., Hoffmann G.F., Donati M.A., Blau N., Wevers R.A.
Ann. Neurol. 62:422-426(2007) [PubMed] [Europe PMC] [Abstract]
Giovanniello T., Leuzzi V., Carducci C., Carducci C., Sabato M.L., Artiola C., Santagata S., Pozzessere S., Antonozzi I.
Neuropediatrics 38:213-215(2007) [PubMed] [Europe PMC] [Abstract]
Wu Z.Y., Lin Y., Chen W.J., Zhao G.X., Xie H., Murong S.X., Wang N.
Clin. Genet. 74:513-521(2008) [PubMed] [Europe PMC] [Abstract]
Clot F., Grabli D., Cazeneuve C., Roze E., Castelnau P., Chabrol B., Landrieu P., Nguyen K., Ponsot G., Abada M., Doummar D., Damier P., Gil R., Thobois S., Ward A.J., Hutchinson M., Toutain A., Picard F. , Camuzat A., Fedirko E., San C., Bouteiller D., LeGuern E., Durr A., Vidailhet M., Brice A.
Brain 132:1753-1763(2009) [PubMed] [Europe PMC] [Abstract]
Willemsen M.A., Verbeek M.M., Kamsteeg E.J., de Rijk-van Andel J.F., Aeby A., Blau N., Burlina A., Donati M.A., Geurtz B., Grattan-Smith P.J., Haeussler M., Hoffmann G.F., Jung H., de Klerk J.B., van der Knaap M.S., Kok F., Leuzzi V., de Lonlay P. , Megarbane A., Monaghan H., Renier W.O., Rondot P., Ryan M.M., Seeger J., Smeitink J.A., Steenbergen-Spanjers G.C., Wassmer E., Weschke B., Wijburg F.A., Wilcken B., Zafeiriou D.I., Wevers R.A.
Brain 133:1810-1822(2010) [PubMed] [Europe PMC] [Abstract]
Mak C.M., Lam C.W., Siu T.S., Chan K.Y., Siu W.K., Yeung W.L., Hui J., Wong V.C., Low L.C., Ko C.H., Fung C.W., Chen S.P., Yuen Y.P., Lee H.C., Yau E., Chan B., Tong S.F., Tam S., Chan Y.W.
Mol. Genet. Metab. 99:431-433(2010) [PubMed] [Europe PMC] [Abstract]
Haugarvoll K., Bindoff L.A.
J. Parkinson's Dis. 1:119-122(2011) [PubMed] [Europe PMC] [Abstract]
Giovanniello T., Claps D., Carducci C., Carducci C., Blau N., Vigevano F., Antonozzi I., Leuzzi V.
J. Child Neurol. 27:523-525(2012) [PubMed] [Europe PMC] [Abstract]
Stamelou M., Mencacci N.E., Cordivari C., Batla A., Wood N.W., Houlden H., Hardy J., Bhatia K.P.
Neurology 79:435-441(2012) [PubMed] [Europe PMC] [Abstract]
Chi C.S., Lee H.F., Tsai C.R.
Pediatr. Neurol. 46:77-82(2012) [PubMed] [Europe PMC] [Abstract]
Cai C., Shi W., Zeng Z., Zhang M., Ling C., Chen L., Cai C., Zhang B., Li W.D.
PLoS ONE 8:E65215-E65215(2013) [PubMed] [Europe PMC] [Abstract]
Fossbakk A., Kleppe R., Knappskog P.M., Martinez A., Haavik J.
Hum. Mutat. 35:880-890(2014) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072863 | 207 | C → Y in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072864 | 227 | D → G in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014026 | 233 | R → H in ARSEGS; loss of over 80% of tyrosine hydroxylase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014027 | 236 | L → P in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and catalytic activity; rare mutation. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072865 | 241 | A → T in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072866 | 246 | H → Y in ARSEGS; loss of about 40% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072867 | 247 | G → S in ARSEGS; loss of about 50% of tyrosine hydroxylase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071715 | 251 | P → L in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072868 | 259 | E → G in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014028 | 276 | T → P in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071716 | 279 | C → F in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072869 | 294 | G → R in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071717 | 296 | R → Q in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072870 | 301 | P → A in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072871 | 309 | F → S in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014029 | 314 | T → M in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071718 | 315 | G → S in ARSEGS. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072872 | 319 | R → P in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072873 | 328 | R → W in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014030 | 337 | R → H in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072874 | 359 | C → F in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072875 | 375 | F → L in ARSEGS; loss of over 80% of tyrosine hydroxylase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072876 | 376 | A → V in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071719 | 382 | I → T in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072877 | 385 | A → V in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072878 | 387 | L → M in ARSEGS; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072879 | 394 | I → T in ARSEGS; complete loss of tyrosine hydroxylase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072880 | 399 | T → M in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072881 | 408 | G → R in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014031 | 412 | Q → K in ARSEGS; loss of over 80% of tyrosine hydroxylase activity; reduced affinity for L-tyrosine. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072882 | 414 | G → R in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071720 | 428 | G → R in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D). 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072883 | 441 | R → P in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072884 | 467 | S → G in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072885 | 492 | P → L in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014032 | 494 | T → M in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072886 | 498 | D → G in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072887 | 510 | L → Q in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"A rare novel deletion of the tyrosine hydroxylase gene in Parkinson disease."
Bademci G., Edwards T.L., Torres A.L., Scott W.K., Zuchner S., Martin E.R., Vance J.M., Wang L.
Hum. Mutat. 31:E1767-E1771(2010) [PubMed] [Europe PMC] [Abstract]Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutation, Dystonia, Parkinson disease, ParkinsonismOrganism-specific databases
DisGeNET More...DisGeNETi | 7054 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | TH |
MalaCards human disease database More...MalaCardsi | TH |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 605407 phenotype |
Open Targets More...OpenTargetsi | ENSG00000180176 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 101150 Autosomal recessive dopa-responsive dystonia |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA351 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1969 |
Drug and drug target database More...DrugBanki | DB00120 L-Phenylalanine DB00135 L-Tyrosine DB03552 Meta-Tyrosine DB00765 Metyrosine DB00360 Sapropterin |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TH |
Domain mapping of disease mutations (DMDM) More...DMDMi | 239938945 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000205561 | 1 – 528 | Tyrosine 3-monooxygenaseAdd BLAST | 528 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 19 | Phosphoserine; by CaMK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 62 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 71 | Phosphoserine; by CaMK2 and PKA1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 502 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
PhosphoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P07101 |
PeptideAtlas More...PeptideAtlasi | P07101 |
PRoteomics IDEntifications database More...PRIDEi | P07101 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51950 51951 [P07101-2] 51952 [P07101-3] 51953 [P07101-4] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P07101 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P07101 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000180176 |
CleanEx database of gene expression profiles More...CleanExi | HS_TH |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P07101 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P07101 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB002522 CAB072340 HPA013768 HPA061003 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- enzyme binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein domain specific binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112912, 13 interactors |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P07101 |
Protein interaction database and analysis system More...IntActi | P07101, 14 interactors |
Molecular INTeraction database More...MINTi | P07101 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000370571 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07101 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 201 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 216 – 218 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 223 – 226 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 228 – 243 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 257 – 277 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 280 – 292 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 303 – 314 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 317 – 320 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 327 – 334 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 335 – 337 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 338 – 341 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 359 – 365 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 367 – 370 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 373 – 386 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 391 – 403 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 404 – 407 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 409 – 412 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 415 – 418 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 421 – 424 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 427 – 433 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 435 – 442 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 445 – 449 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 455 – 457 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 460 – 466 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 468 – 480 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 485 – 491 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 492 – 495 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 496 – 500 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 503 – 526 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 24 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07101 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07101 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 85 – 90 | Poly-Ala | 6 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3820 Eukaryota COG3186 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000010268 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233373 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006841 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P07101 |
KEGG Orthology (KO) More...KOi | K00501 |
Identification of Orthologs from Complete Genome Data More...OMAi | PHLEYFV |
Database of Orthologous Groups More...OrthoDBi | EOG091G05MZ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P07101 |
TreeFam database of animal gene trees More...TreeFami | TF313327 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.800.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001273 ArAA_hydroxylase IPR018301 ArAA_hydroxylase_Fe/CU_BS IPR036951 ArAA_hydroxylase_sf IPR036329 Aro-AA_hydroxylase_C_sf IPR019774 Aromatic-AA_hydroxylase_C IPR005962 Tyr_3_mOase IPR019773 Tyrosine_3-monooxygenase-like IPR021164 Tyrosine_hydroxylase_CS |
The PANTHER Classification System More...PANTHERi | PTHR11473 PTHR11473, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00351 Biopterin_H, 1 hit PF12549 TOH_N, 3 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000336 TH, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00372 FYWHYDRXLASE |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56534 SSF56534, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01269 Tyr_3_monoox, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00367 BH4_AAA_HYDROXYL_1, 1 hit PS51410 BH4_AAA_HYDROXYL_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM VRGQGAPGPS LTGSPWPGTA
60 70 80 90 100
APAASYTPTP RSPRFIGRRQ SLIEDARKER EAAVAAAAAA VPSEPGDPLE
110 120 130 140 150
AVAFEEKEGK AVLNLLFSPR ATKPSALSRA VKVFETFEAK IHHLETRPAQ
160 170 180 190 200
RPRAGGPHLE YFVRLEVRRG DLAALLSGVR QVSEDVRSPA GPKVPWFPRK
210 220 230 240 250
VSELDKCHHL VTKFDPDLDL DHPGFSDQVY RQRRKLIAEI AFQYRHGDPI
260 270 280 290 300
PRVEYTAEEI ATWKEVYTTL KGLYATHACG EHLEAFALLE RFSGYREDNI
310 320 330 340 350
PQLEDVSRFL KERTGFQLRP VAGLLSARDF LASLAFRVFQ CTQYIRHASS
360 370 380 390 400
PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS DEEIEKLSTL
410 420 430 440 450
YWFTVEFGLC KQNGEVKAYG AGLLSSYGEL LHCLSEEPEI RAFDPEAAAV
460 470 480 490 500
QPYQDQTYQS VYFVSESFSD AKDKLRSYAS RIQRPFSVKF DPYTLAIDVL
510 520
DSPQAVRRSL EGVQDELDTL AHALSAIG
The sequence of this isoform differs from the canonical sequence as follows:
31-34: Missing.
10 20 30 40 50
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM GAPGPSLTGS PWPGTAAPAA
60 70 80 90 100
SYTPTPRSPR FIGRRQSLIE DARKEREAAV AAAAAAVPSE PGDPLEAVAF
110 120 130 140 150
EEKEGKAVLN LLFSPRATKP SALSRAVKVF ETFEAKIHHL ETRPAQRPRA
160 170 180 190 200
GGPHLEYFVR LEVRRGDLAA LLSGVRQVSE DVRSPAGPKV PWFPRKVSEL
210 220 230 240 250
DKCHHLVTKF DPDLDLDHPG FSDQVYRQRR KLIAEIAFQY RHGDPIPRVE
260 270 280 290 300
YTAEEIATWK EVYTTLKGLY ATHACGEHLE AFALLERFSG YREDNIPQLE
310 320 330 340 350
DVSRFLKERT GFQLRPVAGL LSARDFLASL AFRVFQCTQY IRHASSPMHS
360 370 380 390 400
PEPDCCHELL GHVPMLADRT FAQFSQDIGL ASLGASDEEI EKLSTLYWFT
410 420 430 440 450
VEFGLCKQNG EVKAYGAGLL SSYGELLHCL SEEPEIRAFD PEAAAVQPYQ
460 470 480 490 500
DQTYQSVYFV SESFSDAKDK LRSYASRIQR PFSVKFDPYT LAIDVLDSPQ
510 520
AVRRSLEGVQ DELDTLAHAL SAIG
The sequence of this isoform differs from the canonical sequence as follows:
31-61: Missing.
10 20 30 40 50
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE
60 70 80 90 100
AAVAAAAAAV PSEPGDPLEA VAFEEKEGKA VLNLLFSPRA TKPSALSRAV
110 120 130 140 150
KVFETFEAKI HHLETRPAQR PRAGGPHLEY FVRLEVRRGD LAALLSGVRQ
160 170 180 190 200
VSEDVRSPAG PKVPWFPRKV SELDKCHHLV TKFDPDLDLD HPGFSDQVYR
210 220 230 240 250
QRRKLIAEIA FQYRHGDPIP RVEYTAEEIA TWKEVYTTLK GLYATHACGE
260 270 280 290 300
HLEAFALLER FSGYREDNIP QLEDVSRFLK ERTGFQLRPV AGLLSARDFL
310 320 330 340 350
ASLAFRVFQC TQYIRHASSP MHSPEPDCCH ELLGHVPMLA DRTFAQFSQD
360 370 380 390 400
IGLASLGASD EEIEKLSTLY WFTVEFGLCK QNGEVKAYGA GLLSSYGELL
410 420 430 440 450
HCLSEEPEIR AFDPEAAAVQ PYQDQTYQSV YFVSESFSDA KDKLRSYASR
460 470 480 490
IQRPFSVKFD PYTLAIDVLD SPQAVRRSLE GVQDELDTLA HALSAIG
The sequence of this isoform differs from the canonical sequence as follows:
35-61: Missing.
10 20 30 40 50
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM VRGQSPRFIG RRQSLIEDAR
60 70 80 90 100
KEREAAVAAA AAAVPSEPGD PLEAVAFEEK EGKAVLNLLF SPRATKPSAL
110 120 130 140 150
SRAVKVFETF EAKIHHLETR PAQRPRAGGP HLEYFVRLEV RRGDLAALLS
160 170 180 190 200
GVRQVSEDVR SPAGPKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD
210 220 230 240 250
QVYRQRRKLI AEIAFQYRHG DPIPRVEYTA EEIATWKEVY TTLKGLYATH
260 270 280 290 300
ACGEHLEAFA LLERFSGYRE DNIPQLEDVS RFLKERTGFQ LRPVAGLLSA
310 320 330 340 350
RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ
360 370 380 390 400
FSQDIGLASL GASDEEIEKL STLYWFTVEF GLCKQNGEVK AYGAGLLSSY
410 420 430 440 450
GELLHCLSEE PEIRAFDPEA AAVQPYQDQT YQSVYFVSES FSDAKDKLRS
460 470 480 490 500
YASRIQRPFS VKFDPYTLAI DVLDSPQAVR RSLEGVQDEL DTLAHALSAI
G
The sequence of this isoform differs from the canonical sequence as follows:
35-61: Missing.
264-357: Missing.
10 20 30 40 50
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM VRGQSPRFIG RRQSLIEDAR
60 70 80 90 100
KEREAAVAAA AAAVPSEPGD PLEAVAFEEK EGKAVLNLLF SPRATKPSAL
110 120 130 140 150
SRAVKVFETF EAKIHHLETR PAQRPRAGGP HLEYFVRLEV RRGDLAALLS
160 170 180 190 200
GVRQVSEDVR SPAGPKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD
210 220 230 240 250
QVYRQRRKLI AEIAFQYRHG DPIPRVEYTA EEIATWDCCH ELLGHVPMLA
260 270 280 290 300
DRTFAQFSQD IGLASLGASD EEIEKLSTLY WFTVEFGLCK QNGEVKAYGA
310 320 330 340 350
GLLSSYGELL HCLSEEPEIR AFDPEAAAVQ PYQDQTYQSV YFVSESFSDA
360 370 380 390 400
KDKLRSYASR IQRPFSVKFD PYTLAIDVLD SPQAVRRSLE GVQDELDTLA
HALSAIG
The sequence of this isoform differs from the canonical sequence as follows:
31-61: Missing.
264-357: Missing.
10 20 30 40 50
MPTPDATTPQ AKGFRRAVSE LDAKQAEAIM SPRFIGRRQS LIEDARKERE
60 70 80 90 100
AAVAAAAAAV PSEPGDPLEA VAFEEKEGKA VLNLLFSPRA TKPSALSRAV
110 120 130 140 150
KVFETFEAKI HHLETRPAQR PRAGGPHLEY FVRLEVRRGD LAALLSGVRQ
160 170 180 190 200
VSEDVRSPAG PKVPWFPRKV SELDKCHHLV TKFDPDLDLD HPGFSDQVYR
210 220 230 240 250
QRRKLIAEIA FQYRHGDPIP RVEYTAEEIA TWDCCHELLG HVPMLADRTF
260 270 280 290 300
AQFSQDIGLA SLGASDEEIE KLSTLYWFTV EFGLCKQNGE VKAYGAGLLS
310 320 330 340 350
SYGELLHCLS EEPEIRAFDP EAAAVQPYQD QTYQSVYFVS ESFSDAKDKL
360 370 380 390 400
RSYASRIQRP FSVKFDPYTL AIDVLDSPQA VRRSLEGVQD ELDTLAHALS
AIG
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 373 | R → H in AAI43615 (PubMed:15489334).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 401 | Y → S in AAA61179 (PubMed:2887169).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 401 | Y → S in CAA28908 (PubMed:2882428).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 401 | Y → S in CAA68472 (PubMed:2888085).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072862 | 19 | S → C Found in a patient with ARSEGS; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014025 | 112 | V → M Common polymorphism. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072863 | 207 | C → Y in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072864 | 227 | D → G in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014026 | 233 | R → H in ARSEGS; loss of over 80% of tyrosine hydroxylase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014027 | 236 | L → P in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and catalytic activity; rare mutation. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072865 | 241 | A → T in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072866 | 246 | H → Y in ARSEGS; loss of about 40% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072867 | 247 | G → S in ARSEGS; loss of about 50% of tyrosine hydroxylase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071715 | 251 | P → L in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072868 | 259 | E → G in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014028 | 276 | T → P in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071716 | 279 | C → F in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072869 | 294 | G → R in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071717 | 296 | R → Q in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072870 | 301 | P → A in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072871 | 309 | F → S in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014029 | 314 | T → M in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071718 | 315 | G → S in ARSEGS. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072872 | 319 | R → P in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072873 | 328 | R → W in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014030 | 337 | R → H in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072874 | 359 | C → F in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072875 | 375 | F → L in ARSEGS; loss of over 80% of tyrosine hydroxylase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072876 | 376 | A → V in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071719 | 382 | I → T in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072877 | 385 | A → V in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072878 | 387 | L → M in ARSEGS; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072879 | 394 | I → T in ARSEGS; complete loss of tyrosine hydroxylase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072880 | 399 | T → M in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072881 | 408 | G → R in ARSEGS. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014031 | 412 | Q → K in ARSEGS; loss of over 80% of tyrosine hydroxylase activity; reduced affinity for L-tyrosine. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072882 | 414 | G → R in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071720 | 428 | G → R in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D). 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072883 | 441 | R → P in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072884 | 467 | S → G in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072885 | 492 | P → L in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014032 | 494 | T → M in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072886 | 498 | D → G in ARSEGS; loss of over 80% of tyrosine hydroxylase activity. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014033 | 499 | V → M1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072887 | 510 | L → Q in ARSEGS; complete loss of tyrosine hydroxylase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000544 | 31 – 61 | Missing in isoform 2 and isoform 6. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 31 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000543 | 31 – 34 | Missing in isoform 1. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 4 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000541 | 35 – 61 | Missing in isoform 4 and isoform 5. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 27 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_054338 | 264 – 357 | Missing in isoform 5 and isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 94 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M17589 mRNA Translation: AAA61179.1 X05290 mRNA Translation: CAA28908.1 Y00414 mRNA Translation: CAA68472.1 DQ677336 mRNA Translation: ABG73364.1 DQ677337 mRNA Translation: ABG73365.1 AC132217 Genomic DNA No translation available. M24791, M24787, M24789 Genomic DNA Translation: AAA61173.1 Sequence problems. CH471158 Genomic DNA Translation: EAX02493.1 BC104967 mRNA Translation: AAI04968.1 BC143611 mRNA Translation: AAI43612.1 BC143614 mRNA Translation: AAI43615.1 M24791, M24787 Genomic DNA Translation: AAA61170.1 M20911 mRNA Translation: AAA61167.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31338.1 [P07101-2] CCDS7730.1 [P07101-3] CCDS7731.1 [P07101-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A30002 WHHUY4 |
NCBI Reference Sequences More...RefSeqi | NP_000351.2, NM_000360.3 [P07101-3] NP_954986.2, NM_199292.2 [P07101-1] NP_954987.2, NM_199293.2 [P07101-2] XP_011518637.1, XM_011520335.2 [P07101-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.435609 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000333684; ENSP00000328814; ENSG00000180176 [P07101-6] ENST00000352909; ENSP00000325951; ENSG00000180176 [P07101-3] ENST00000381175; ENSP00000370567; ENSG00000180176 [P07101-2] ENST00000381178; ENSP00000370571; ENSG00000180176 [P07101-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 7054 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:7054 |
UCSC genome browser More...UCSCi | uc001lvp.3 human [P07101-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P07101 | Tyrosine 3-monooxygenase type 1 and 2 (Fragment) | 45 | |||
| Tyrosine 3-monooxygenase type 1 and 2 (Fragment) | 45 | ||||
| Tyrosine 3-monooxygenase type 3 and 4 (Fragment) | 27 | ||||
| Tyrosine hydroxylase (Fragment) | 65 | ||||
| Tyrosine hydroxylase (Fragment) | 138 | ||||
| +1 | |||||
| P07101-4 | Tyrosine hydroxylase (Fragment) | 106 | |||
| Tyrosine hydroxylase (Fragment) | 111 | ||||
| P07101-5 | TH isoform 8 (Fragment) | 115 | |||
| TH isoform 8 (Fragment) | 115 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P07101 | Tyrosine 3-monooxygenase type 1 and 2 (Fragment) | 45 | |||
| Tyrosine 3-monooxygenase type 1 and 2 (Fragment) | 45 | ||||
| Tyrosine 3-monooxygenase type 3 and 4 (Fragment) | 27 | ||||
| Tyrosine hydroxylase (Fragment) | 65 | ||||
| Tyrosine hydroxylase | 549 | ||||
| +39 | |||||
| P07101-3 | Tyrosine hydroxylase (Fragment) | 106 | |||
| UPI000533F220 | 576 | ||||
| Tyrosine hydroxylase | 524 | ||||
| UPI000732BA47 | 510 | ||||
| UPI000C2A4AFB | 501 | ||||
| +36 | |||||
| P07101-4 | Tyrosine hydroxylase (Fragment) | 106 | |||
| UPI000533F220 | 576 | ||||
| Tyrosine hydroxylase | 524 | ||||
| UPI000732BA47 | 510 | ||||
| UPI000C2A4AFB | 501 | ||||
| +36 | |||||
| P07101-5 | TH isoform 8 (Fragment) | 115 | |||
| TH isoform 8 (Fragment) | 115 | ||||
| UPI0004D07A64 | 407 | ||||
| UPI000533298D | 407 | ||||
| UPI0005F42E74 | 407 | ||||
| +25 | |||||
| P07101-6 | TH isoform 8 (Fragment) | 115 | |||
| TH isoform 8 (Fragment) | 115 | ||||
| UPI0004D07A64 | 407 | ||||
| UPI000533298D | 407 | ||||
| UPI0005F42E74 | 407 | ||||
| +25 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P07101 | Tyrosine 3-monooxygenase type 1 and 2 (Fragment) | 45 | |||
| Tyrosine 3-monooxygenase type 1 and 2 (Fragment) | 45 | ||||
| Tyrosine 3-monooxygenase type 3 and 4 (Fragment) | 27 | ||||
| Tyrosine hydroxylase (Fragment) | 65 | ||||
| Tyrosine hydroxylase | 549 | ||||
| +197 | |||||
| P07101-5 | TH isoform 8 (Fragment) | 115 | |||
| TH isoform 8 (Fragment) | 115 | ||||
| UPI0005F42E74 | 407 | ||||
| UPI000533298D | 407 | ||||
| UPI0004D07A64 | 407 | ||||
| +28 | |||||
| P07101-6 | TH isoform 8 (Fragment) | 115 | |||
| TH isoform 8 (Fragment) | 115 | ||||
| UPI0005F42E74 | 407 | ||||
| UPI000533298D | 407 | ||||
| UPI0004D07A64 | 407 | ||||
| +28 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Wikipedia Tyrosine hydroxylase entry |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M17589 mRNA Translation: AAA61179.1 X05290 mRNA Translation: CAA28908.1 Y00414 mRNA Translation: CAA68472.1 DQ677336 mRNA Translation: ABG73364.1 DQ677337 mRNA Translation: ABG73365.1 AC132217 Genomic DNA No translation available. M24791, M24787, M24789 Genomic DNA Translation: AAA61173.1 Sequence problems. CH471158 Genomic DNA Translation: EAX02493.1 BC104967 mRNA Translation: AAI04968.1 BC143611 mRNA Translation: AAI43612.1 BC143614 mRNA Translation: AAI43615.1 M24791, M24787 Genomic DNA Translation: AAA61170.1 M20911 mRNA Translation: AAA61167.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31338.1 [P07101-2] CCDS7730.1 [P07101-3] CCDS7731.1 [P07101-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A30002 WHHUY4 |
NCBI Reference Sequences More...RefSeqi | NP_000351.2, NM_000360.3 [P07101-3] NP_954986.2, NM_199292.2 [P07101-1] NP_954987.2, NM_199293.2 [P07101-2] XP_011518637.1, XM_011520335.2 [P07101-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.435609 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2XSN | X-ray | 2.68 | A/B/C/D | 193-528 | [»] | |
| 4J6S | X-ray | 3.08 | E/F/G/H | 1-74 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07101 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07101 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112912, 13 interactors |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P07101 |
Protein interaction database and analysis system More...IntActi | P07101, 14 interactors |
Molecular INTeraction database More...MINTi | P07101 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000370571 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07101 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1969 |
Drug and drug target database More...DrugBanki | DB00120 L-Phenylalanine DB00135 L-Tyrosine DB03552 Meta-Tyrosine DB00765 Metyrosine DB00360 Sapropterin |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P07101 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P07101 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TH |
Domain mapping of disease mutations (DMDM) More...DMDMi | 239938945 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P07101 |
PeptideAtlas More...PeptideAtlasi | P07101 |
PRoteomics IDEntifications database More...PRIDEi | P07101 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51950 51951 [P07101-2] 51952 [P07101-3] 51953 [P07101-4] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000333684; ENSP00000328814; ENSG00000180176 [P07101-6] ENST00000352909; ENSP00000325951; ENSG00000180176 [P07101-3] ENST00000381175; ENSP00000370567; ENSG00000180176 [P07101-2] ENST00000381178; ENSP00000370571; ENSG00000180176 [P07101-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 7054 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:7054 |
UCSC genome browser More...UCSCi | uc001lvp.3 human [P07101-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 7054 |
DisGeNET More...DisGeNETi | 7054 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000180176.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TH |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | TH |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0035928 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11782 TH |
Human Protein Atlas More...HPAi | CAB002522 CAB072340 HPA013768 HPA061003 |
MalaCards human disease database More...MalaCardsi | TH |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 191290 gene 605407 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P07101 |
Open Targets More...OpenTargetsi | ENSG00000180176 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 101150 Autosomal recessive dopa-responsive dystonia |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA351 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3820 Eukaryota COG3186 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000010268 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233373 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006841 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P07101 |
KEGG Orthology (KO) More...KOi | K00501 |
Identification of Orthologs from Complete Genome Data More...OMAi | PHLEYFV |
Database of Orthologous Groups More...OrthoDBi | EOG091G05MZ |
Database for complete collections of gene phylogenies More...PhylomeDBi | P07101 |
TreeFam database of animal gene trees More...TreeFami | TF313327 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00747; UER00733 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.14.16.2 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-209905 Catecholamine biosynthesis |
SIGNOR Signaling Network Open Resource More...SIGNORi | P07101 |
Miscellaneous databases
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Tyrosine_hydroxylase |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 7054 |
Protein Ontology More...PROi | PR:P07101 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000180176 |
CleanEx database of gene expression profiles More...CleanExi | HS_TH |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P07101 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P07101 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.800.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001273 ArAA_hydroxylase IPR018301 ArAA_hydroxylase_Fe/CU_BS IPR036951 ArAA_hydroxylase_sf IPR036329 Aro-AA_hydroxylase_C_sf IPR019774 Aromatic-AA_hydroxylase_C IPR005962 Tyr_3_mOase IPR019773 Tyrosine_3-monooxygenase-like IPR021164 Tyrosine_hydroxylase_CS |
The PANTHER Classification System More...PANTHERi | PTHR11473 PTHR11473, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00351 Biopterin_H, 1 hit PF12549 TOH_N, 3 hits |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000336 TH, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00372 FYWHYDRXLASE |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56534 SSF56534, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01269 Tyr_3_monoox, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00367 BH4_AAA_HYDROXYL_1, 1 hit PS51410 BH4_AAA_HYDROXYL_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | TY3H_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P07101Primary (citable) accession number: P07101 Secondary accession number(s): B7ZL70 , B7ZL73, Q0PWM2, Q0PWM3, Q15585, Q15588, Q15589, Q2M3B4 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
| Last sequence update: | June 16, 2009 | |
| Last modified: | July 18, 2018 | |
| This is version 205 of the entry and version 5 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
